Evidence map›Paper›PMID 25330043›Full record

ArticlePLoS genetics2014

Functional interaction between ribosomal protein L6 and RbgA during ribosome assembly.

Megha Gulati, Nikhil Jain, Joseph H Davis, James R Williamson, Robert A Britton

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 31 citations in OpenAlex.

  1. The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. The GTPase BipA expressed at low temperature inThe Journal of biological chemistry · 2018
    Article
  14. Article
  15. Article
  16. Structure and dynamics of bacterial ribosome biogenesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Megha GulatiDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan, United States of America.
Nikhil JainDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan, United States of America.
Joseph H DavisDepartment of Integrative Structural and Computational Biology, Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, United States of America.
James R WilliamsonDepartment of Integrative Structural and Computational Biology, Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, United States of America.
Robert A BrittonDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan, United States of America.
Michigan State University · USScripps Research Institute · US

Funding

Assembly of E. coli ribosomes in vitro and in cellsR37GM053757 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILLIAMSON, JAMES R · 2008 to 2017
$5.1M
GTPase control of large ribosome subunit biogenesisR01GM110248 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BRITTON, ROBERT A · 2015 to 2018
$1.5M
NIGMS NIH HHS R01 GM110248NIGMS NIH HHS R37 GM053757
6 · The paper itself

Abstract

RbgA is an essential GTPase that participates in the assembly of the large ribosomal subunit in Bacillus subtilis and its homologs are implicated in mitochondrial and eukaryotic large subunit assembly. How RbgA functions in this process is still poorly understood. To gain insight into the function of RbgA we isolated suppressor mutations that partially restored the growth of an RbgA mutation (RbgA-F6A) that caused a severe growth defect. Analysis of these suppressors identified mutations in rplF, encoding ribosomal protein L6. The suppressor strains all accumulated a novel ribosome intermediate that migrates at 44S in sucrose gradients. All of the mutations cluster in a region of L6 that is in close contact with helix 97 of the 23S rRNA. In vitro maturation assays indicate that the L6 substitutions allow the defective RbgA-F6A protein to function more effectively in ribosome maturation. Our results suggest that RbgA functions to properly position L6 on the ribosome, prior to the incorporation of L16 and other late assembly proteins.

Indexed as

Bacillus subtilisBacterial ProteinsRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialRNA, Ribosomal, 23SSuppression, GeneticBacterial Proteinsribosomal protein L16ribosomal protein L6Ribosomal ProteinsRNA, Ribosomal, 23S

Identifiers

PMID25330043
PMCPMC4199504
OpenAlexW2014846856

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.